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. 2022 Jan;14(1):9-16.
doi: 10.4155/fmc-2021-0216. Epub 2021 Nov 3.

Candesartan, losartan and valsartan Zn(II) complexes interactions with bovine serum albumin

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Candesartan, losartan and valsartan Zn(II) complexes interactions with bovine serum albumin

Valeria R Martínez et al. Future Med Chem. 2022 Jan.

Abstract

Background: The pharmacological response and the therapeutic efficacy of a drug depends on the interactions with plasma proteins. Methodology: The interaction of bovine serum albumin (BSA) with the metal complexes of antihypertensive drugs, Zn(II)/sartan complexes (candesartan, valsartan and losartan), was investigated using fluorescence quenching determinations at different temperatures. Results: The binding studies of the compounds with BSA showed static quenching and moderate binding with calculated constants in the range of 104-106 M-1, indicating potent serum distribution via albumins. In all cases, negative values of free energy are indicative of spontaneous processes and the stabilization of BSA/compound complexes through hydrogen bonding and van der Waals forces. The results for the sartans agree with the reported pharmacokinetics studies. Conclusion: It has been determined that the three sartans and the Zn complexes could be transported and distributed by albumin.

Keywords: Zn(II) metal complex; angiotensin II receptor blockers; bovine serum albumin.

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